Characterization of C-terminal structure of MinC and its implication in evolution of bacterial cell division.

ABSTRACT: Proper cell division at the mid-site of Gram-negative bacteria reflects stringent regulation by the min system (MinC, MinD and MinE). Herein we report crystal structure of the C-terminal domain of MinC from Escherichia coli (EcMinC_CTD). The MinC_CTD beta helical domain is engaged in a tight homodimer, similar to Thermotoga maritima MinC_CTD (TmMinC_CTD). However, both EcMinC_CTD and TmMinC_CTD lack an α-helix (helix3) at their C-terminal tail, in comparison to Aquifex aerolicu MinC_CTD (AaMinC_CTD) which forms an extra interaction interface with MinD. To understand the role of this extra binding element in MinC/MinD interactions, we fused this helix (Aahelix3) to the C-terminus of EcMinC and examined its effec

SUBMITTER: Yang S 

PROVIDER: S-EPMC5548801 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature